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Volumn 34, Issue 5-6, 1999, Pages 483-486

Is the rate of sulfur-disulfide exchange between the native β-lactoglobulin and PDS related to protein conformational stability?

Author keywords

Dimer dissociation; Dynamics; Flexibility; Sulphur disulphide exchange; Lactoglobulin

Indexed keywords


EID: 0039846338     PISSN: 09505423     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2621.1999.00390.x     Document Type: Article
Times cited : (3)

References (11)
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  • 2
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  • 3
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    • Protein stability function relations: Sulfhydryl-disulfide exchange in native β-lactoglobulin
    • submitted
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  • 4
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  • 5
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    • Harrison, P.M.1    Chan, H.S.2    Pruisner, S.B.3    Cohen, F.E.4
  • 9
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    • Flexibility: The key to p53 function?
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  • 11
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.